ABCC7 p.Asn1303Ala
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PMID: 11788611
[PubMed]
Berger AL et al: "Mutations that change the position of the putative gamma-phosphate linker in the nucleotide binding domains of CFTR alter channel gating."
No.
Sentence
Comment
161
We observed similar kinetic effects when Asn-1303 was changed to another CF-associated mutation (N1303H), a sequenced mutation with undetermined clinical consequences (N1303I), and an Ala (N1303A) (Fig. 8).
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ABCC7 p.Asn1303Ala 11788611:161:189
status: NEW171 However, in contrast to the reduced EC50 for ATP observed for mutations at Lys-1250 (21), the apparent EC50 for CFTR-N1303A (253 Ϯ 62 M, n ϭ 5) was not different from that of wild type CFTR (176 Ϯ 67 M, n ϭ 5).
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ABCC7 p.Asn1303Ala 11788611:171:117
status: NEW180 Comparison of single-channel kinetics of CFTR-N1303K, CFTR-N1303H, CFTR-N1303I, and CFTR-N1303A.
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ABCC7 p.Asn1303Ala 11788611:180:89
status: NEW
PMID: 14697202
[PubMed]
Randak C et al: "An intrinsic adenylate kinase activity regulates gating of the ABC transporter CFTR."
No.
Sentence
Comment
262
We also made the corresponding mutations in CFTR of ATP, and agrees with our earlier finding that wild-type and N1303A CFTR had the same ATP EC50 for current and examined their effect on channel activity.
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ABCC7 p.Asn1303Ala 14697202:262:112
status: NEW